Abstract
Unconventional myosins are a large superfamily of actin-based molecular motors that use ATP as fuel to generate mechanical motions/forces. The distinct tails in different unconventional myosin subfamilies can recognize various cargoes including proteins and lipids. Thus, they can play diverse roles in many biological processes such as cellular trafficking, mechanical supports, force sensing, etc. This chapter focuses on some recent advances on the structural studies of how unconventional myosins specifically bind to cargoes with their cargo-binding domains.
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Acknowledgments
We thank Dr. Zhe Feng of the M. Z. laboratory for critical reading and editing. Research described in this work from our laboratory was supported by grants from RGC of Hong Kong (16149516 and many completed ones) to M.Z. We thank many of our past members of the laboratory for their contributions to the work described in this piece. We apologize to the authors whose papers have not been cited due to limited space of this review chapter. M.Z. is a Kerry Holdings Professor in Science and a Senior Fellow of IAS at HKUST.
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Li, J., Zhang, M. (2020). Cargo Binding by Unconventional Myosins. In: Coluccio, L. (eds) Myosins. Advances in Experimental Medicine and Biology, vol 1239. Springer, Cham. https://doi.org/10.1007/978-3-030-38062-5_3
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